Search Results

Overview

Uniprot IDO96019
Protein NameActin-like protein 6A
Gene NameACTL6A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
242 ANWKRKEKLPQVTRS
34 YAGEDCPKVDFPTAI

Function

Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair

Protein Sequence

10 MSGGVYGGDE 20 VGALVFDIGS 30 YTVRAGYAGE 40 DCPKVDFPTA 50 IGMVVERDDG 60 STLMEIDGDK 70 GKQGGPTYYI 80 DTNALRVPRE 90 NMEAISPLKN 100 GMVEDWDSFQ 110 AILDHTYKMH 120 VKSEASLHPV 130 LMSEAPWNTR 140 AKREKLTELM 150 FEHYNIPAFF 160 LCKTAVLTAF 170 ANGRSTGLIL 180 DSGATHTTAI 190 PVHDGYVLQQ 200 GIVKSPLAGD 210 FITMQCRELF 220 QEMNIELVPP 230 YMIASKEAVR 240 EGSPANWKRK 250 EKLPQVTRSW 260 HNYMCNCVIQ 270 DFQASVLQVS 280 DSTYDEQVAA 290 QMPTVHYEFP 300 NGYNCDFGAE 310 RLKIPEGLFD 320 PSNVKGLSGN 330 TMLGVSHVVT 340 TSVGMCDIDI 350 RPGLYGSVIV 360 AGGNTLIQSF 370 TDRLNRELSQ 380 KTPPSMRLKL 390 IANNTTVERR 400 FSSWIGGSIL 410 ASLGTFQQMW 420 ISKQEYEEGG KQCVERKCP

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Biological Process GO:0007399 nervous system development
Biological Process GO:0003407 neural retina development
Biological Process GO:0045597 positive regulation of cell differentiation
Biological Process GO:0008284 positive regulation of cell population proliferation
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:2000781 positive regulation of double-strand break repair
Biological Process GO:1905168 positive regulation of double-strand break repair via homologous recombination
Biological Process GO:0045663 positive regulation of myoblast differentiation
Biological Process GO:1902459 positive regulation of stem cell population maintenance
Biological Process GO:0045582 positive regulation of T cell differentiation
Biological Process GO:1904507 positive regulation of telomere maintenance in response to DNA damage
Biological Process GO:0042981 regulation of apoptotic process
Biological Process GO:0051726 regulation of cell cycle
Biological Process GO:0033044 regulation of chromosome organization
Biological Process GO:0006275 regulation of DNA replication
Biological Process GO:0060382 regulation of DNA strand elongation
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:2000779 regulation of double-strand break repair
Biological Process GO:0045995 regulation of embryonic development
Biological Process GO:0070316 regulation of G0 to G1 transition
Biological Process GO:2000045 regulation of G1/S transition of mitotic cell cycle
Biological Process GO:0030071 regulation of mitotic metaphase/anaphase transition
Biological Process GO:2000819 regulation of nucleotide-excision repair
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0007165 signal transduction
Biological Process GO:0021510 spinal cord development
Biological Process GO:0000723 telomere maintenance
Cellular Component GO:0031011 Ino80 complex
Cellular Component GO:0000776 kinetochore
Cellular Component GO:0071564 npBAF complex
Cellular Component GO:0035267 NuA4 histone acetyltransferase complex
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0016514 SWI/SNF complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003713 transcription coactivator activity
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0006310 DNA recombination
Biological Process GO:0006281 DNA repair
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0045596 negative regulation of cell differentiation

Reference

[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.